PMID- 10318784
OWN - NLM
STAT- MEDLINE
DCOM- 19990617
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 20
DP  - 1999 May 14
TI  - Molecular cloning and structural and functional characterization of human
      cathepsin F, a new cysteine proteinase of the papain family with a long
      propeptide domain.
PG  - 13800-9
AB  - A cDNA encoding a new cysteine proteinase belonging to the papain family and
      called cathepsin F has been cloned from a human prostate cDNA library. This cDNA 
      encodes a polypeptide of 484 amino acids, with the same domain organization as
      other cysteine proteinases, including a hydrophobic signal sequence, a prodomain,
      and a catalytic region. However, this propeptide domain is unusually long and
      distinguishes cathepsin F from other proteinases of the papain family. Cathepsin 
      F also shows all structural motifs characteristic of these proteinases, including
      the essential cysteine residue of the active site. Consistent with these
      structural features, cathepsin F produced in Escherichia coli as a fusion protein
      with glutathione S-transferase degrades the synthetic peptide
      benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin, a substrate commonly used for
      functional characterization of cysteine proteinases. Furthermore, this
      proteolytic activity is blocked by
      trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, an inhibitor of cysteine
      proteinases. The gene encoding cathepsin F maps to chromosome 11q13, close to
      that encoding cathepsin W. Cathepsin F is widely expressed in human tissues,
      suggesting a role in normal protein catabolism. Northern blot analysis also
      revealed a significant level of expression in some cancer cell lines opening the 
      possibility that this enzyme could be involved in degradative processes occurring
      during tumor progression.
FAU - Santamaria, I
AU  - Santamaria I
AD  - Departamento de Bioquimica y Biologia Molecular, Facultad de Medicina,
      Universidad de Oviedo, 33006-Oviedo, Spain.
FAU - Velasco, G
AU  - Velasco G
FAU - Pendas, A M
AU  - Pendas AM
FAU - Paz, A
AU  - Paz A
FAU - Lopez-Otin, C
AU  - Lopez-Otin C
LA  - eng
SI  - GENBANK/AJ007331
SI  - GENBANK/AJ131851
SI  - GENBANK/H39591
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Recombinant Proteins)
RN  - EC 3.4.- (Cathepsins)
RN  - EC 3.4.22.41 (CTSF protein, human)
RN  - EC 3.4.22.41 (Cathepsin F)
RN  - EC 3.4.22.41 (Ctsf protein, mouse)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cathepsin F
MH  - Cathepsins/chemistry/*genetics/*physiology
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - Escherichia coli
MH  - Genomic Library
MH  - Humans
MH  - Male
MH  - Mice
MH  - Molecular Sequence Data
MH  - Prostate/chemistry
MH  - Protein Conformation
MH  - Recombinant Proteins/biosynthesis
MH  - Sequence Alignment
MH  - Structure-Activity Relationship
MH  - Tumor Cells, Cultured
EDAT- 1999/05/13 00:00
MHDA- 1999/05/13 00:01
CRDT- 1999/05/13 00:00
PHST- 1999/05/13 00:00 [pubmed]
PHST- 1999/05/13 00:01 [medline]
PHST- 1999/05/13 00:00 [entrez]
AID - 10.1074/jbc.274.20.13800 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 May 14;274(20):13800-9. doi: 10.1074/jbc.274.20.13800.